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A zinc complex of heparan sulfate destabilises lysozyme and alters its conformation

DOI: 10.1016/j.bbrc.2012.07.154 DOI Help

Authors: Ashley Hughes (University of Liverpool) , Rohanah Hussain (Diamond Light Source) , Cesare Cosentino (Istituto di Ricerche Chimiche e Biochimiche) , Marco Guerrini (Istituto di Ricerche Chimiche e Biochimiche) , Giuliano Siligardi (Diamond Light Source) , Edwin Yates (University of Liverpool) , Timothy Rudd (University of Liverpool)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biochemical And Biophysical Research Communications , VOL 425 (4) , PAGES 794 - 799

State: Published (Approved)
Published: September 2012

Abstract: The naturally occurring anionic cell surface polysaccharide heparan sulfate is involved in key biological activities and is implicated in amyloid formation. Following addition of Zn–heparan sulfate, hen lysozyme, a model amyloid forming protein, resembled ?-rich amyloid by far UV circular dichroism (increased ?-sheet: +25%), with a significantly reduced melting temperature (from 68 to 58 °C) by fluorescence shift assay. Secondary structure stability of the Zn–heparan sulfate complex with lysozyme was also distinct from that with heparan sulfate, under stronger denaturation conditions using synchrotron radiation circular dichroism. Changing the cation associated with heparan sulfate is sufficient to alter the conformation and stability of complexes formed between heparan sulfate and lysozyme, substantially reducing the stability of the protein. Complexes of heparan sulfate and cations, such as Zn, which are abundant in the brain, may provide alternative folding routes for proteins.

Journal Keywords: Brain; Cations; Chickens; Dichroism; Fluorescence; Lysozyme; Melting Points; Polysaccharides; Sulfates; Synchrotron Radiation; Zinc; Zinc Complexes

Subject Areas: Biology and Bio-materials

Instruments: B23-Circular Dichroism